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Database: UniProt
Entry: A0A0U5C632_9EURO
LinkDB: A0A0U5C632_9EURO
Original site: A0A0U5C632_9EURO 
ID   A0A0U5C632_9EURO        Unreviewed;       690 AA.
AC   A0A0U5C632;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ASPCAL04838 {ECO:0000313|EMBL:CEL03692.1};
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=454130 {ECO:0000313|EMBL:CEL03692.1, ECO:0000313|Proteomes:UP000054771};
RN   [1] {ECO:0000313|EMBL:CEL03692.1, ECO:0000313|Proteomes:UP000054771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CDMC01000004; CEL03692.1; -; Genomic_DNA.
DR   EnsemblFungi; CEL03692; CEL03692; ASPCAL04838.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054771; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054771};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054771};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    690       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006855606.
FT   DOMAIN      397    579       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   690 AA;  77235 MW;  8FB2E4B9A118D032 CRC64;
     MRLWHTLGRG LAIAGLASQA TAQDWPLHDN GLNKVVQWDH YSVMVNGERL FLWSGELHLW
     RIPVPELWRD IFQKIKAAGF NGIGLYEHWG WHAPNNETLD FETGAHDFAK AFDIAQEVGL
     YIVYRPGPYS NAEANGGGFP GWLTTGEYGP LRDNSTEYTK AWTRYSGAVA EYVRPYLITN
     GGPIIMWQIE NEYGVQWIDQ ETRTPNETAV HYMELLEEKH RGWGIDVPFT ANNPNMWTRS
     WSKDFSNVGG EADVYGLDHY PACWTCNLEQ CLPVNGQVEP YTVFDYYSHF QEVAQTQPSF
     LMEFQGGSFN PWDGPAGGCR ENMGPGWVNL FFRHNLAQKV SAVNIYMLYG GTNWGNIGFP
     EVGTSYDYSA PIHENRLISD KYSESKLFGL FMRVARDFTK VERVGNSTAY ATDSDIFTAE
     LRNPDTDAAY YVVRHDYSPS TEVTKFRLDV STEIGDLTVP SRGSITLNGT ESKVLVTDFS
     IGSSGKKITY ATLEVLTVAD LGDRQVVVFW APEGEEGEFL LKGAKSGRVV SGNADTKRTL
     TKTRNGVVAN VVTGEEKLVI DYNNHVQAVV VDRQGAYKFW APTLDNDPLA WENSTVLVQG
     PYLIRTAEIK GDTIHITGDW NEETDVDIWA PKRVKKVTFN GSKLRVTKSK YGTLIGTLPA
     PEVTLESLAA NLPPLTEWKV ADNLPEAATD
//
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